RHBL1_HUMAN
ID RHBL1_HUMAN Reviewed; 438 AA.
AC O75783; A2IDC0; A2IDC1; Q0VAX4; Q9NQ85;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Rhomboid-related protein 1;
DE Short=RRP;
DE EC=3.4.21.105;
DE AltName: Full=Rhomboid-like protein 1;
GN Name=RHBDL1; Synonyms=RHBDL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Leukemia;
RX PubMed=9662444; DOI=10.1016/s0014-5793(98)00622-x;
RA Pascall J.C., Brown K.D.;
RT "Characterization of a mammalian cDNA encoding a protein with high sequence
RT similarity to the Drosophila regulatory protein Rhomboid.";
RL FEBS Lett. 429:337-340(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May be involved in regulated intramembrane proteolysis and
CC the subsequent release of functional polypeptides from their membrane
CC anchors. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleaves type-1 transmembrane domains using a catalytic dyad
CC composed of serine and histidine that are contributed by different
CC transmembrane domains.; EC=3.4.21.105;
CC -!- INTERACTION:
CC O75783; O95870: ABHD16A; NbExp=3; IntAct=EBI-12104986, EBI-348517;
CC O75783; P05090: APOD; NbExp=3; IntAct=EBI-12104986, EBI-715495;
CC O75783; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-12104986, EBI-12003442;
CC O75783; P21964: COMT; NbExp=3; IntAct=EBI-12104986, EBI-372265;
CC O75783; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-12104986, EBI-713304;
CC O75783; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-12104986, EBI-10171774;
CC O75783; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-12104986, EBI-14065470;
CC O75783; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-12104986, EBI-11956541;
CC O75783; Q969W0: SPTSSA; NbExp=3; IntAct=EBI-12104986, EBI-723396;
CC O75783; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-12104986, EBI-11988865;
CC O75783; Q08AM6: VAC14; NbExp=3; IntAct=EBI-12104986, EBI-2107455;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75783-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75783-2; Sequence=VSP_005372;
CC -!- TISSUE SPECIFICITY: Detected in heart, brain, skeletal muscle and
CC kidney.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
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DR EMBL; Y17108; CAA76629.1; -; mRNA.
DR EMBL; AJ272344; CAC00640.1; -; mRNA.
DR EMBL; AE006464; AAK61241.1; -; Genomic_DNA.
DR EMBL; Z92544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85760.1; -; Genomic_DNA.
DR EMBL; BC120874; AAI20875.1; -; mRNA.
DR EMBL; BC120875; AAI20876.1; -; mRNA.
DR CCDS; CCDS10418.1; -. [O75783-1]
DR CCDS; CCDS61779.1; -. [O75783-2]
DR RefSeq; NP_001265649.1; NM_001278720.1. [O75783-2]
DR RefSeq; NP_001265650.1; NM_001278721.1.
DR RefSeq; NP_001305662.1; NM_001318733.1. [O75783-1]
DR AlphaFoldDB; O75783; -.
DR SMR; O75783; -.
DR BioGRID; 114495; 18.
DR IntAct; O75783; 15.
DR STRING; 9606.ENSP00000344206; -.
DR MEROPS; S54.005; -.
DR iPTMnet; O75783; -.
DR PhosphoSitePlus; O75783; -.
DR BioMuta; RHBDL1; -.
DR MassIVE; O75783; -.
DR PaxDb; O75783; -.
DR PeptideAtlas; O75783; -.
DR PRIDE; O75783; -.
DR ProteomicsDB; 50193; -. [O75783-1]
DR ProteomicsDB; 50194; -. [O75783-2]
DR Antibodypedia; 22802; 31 antibodies from 13 providers.
DR DNASU; 9028; -.
DR Ensembl; ENST00000219551.2; ENSP00000219551.2; ENSG00000103269.14. [O75783-1]
DR Ensembl; ENST00000352681.8; ENSP00000344206.3; ENSG00000103269.14. [O75783-2]
DR GeneID; 9028; -.
DR KEGG; hsa:9028; -.
DR MANE-Select; ENST00000352681.8; ENSP00000344206.3; NM_001278720.2; NP_001265649.1. [O75783-2]
DR UCSC; uc002cir.2; human. [O75783-1]
DR CTD; 9028; -.
DR DisGeNET; 9028; -.
DR GeneCards; RHBDL1; -.
DR HGNC; HGNC:10007; RHBDL1.
DR HPA; ENSG00000103269; Tissue enhanced (brain).
DR MIM; 603264; gene.
DR neXtProt; NX_O75783; -.
DR OpenTargets; ENSG00000103269; -.
DR PharmGKB; PA34382; -.
DR VEuPathDB; HostDB:ENSG00000103269; -.
DR eggNOG; KOG2289; Eukaryota.
DR GeneTree; ENSGT00940000160651; -.
DR HOGENOM; CLU_048023_2_1_1; -.
DR InParanoid; O75783; -.
DR OMA; VFMCYGV; -.
DR OrthoDB; 1253228at2759; -.
DR PhylomeDB; O75783; -.
DR TreeFam; TF313540; -.
DR PathwayCommons; O75783; -.
DR SignaLink; O75783; -.
DR BioGRID-ORCS; 9028; 9 hits in 961 CRISPR screens.
DR GenomeRNAi; 9028; -.
DR Pharos; O75783; Tdark.
DR PRO; PR:O75783; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O75783; protein.
DR Bgee; ENSG00000103269; Expressed in right hemisphere of cerebellum and 94 other tissues.
DR ExpressionAtlas; O75783; baseline and differential.
DR Genevisible; O75783; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.20.1540.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR Pfam; PF01694; Rhomboid; 1.
DR SUPFAM; SSF144091; SSF144091; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Membrane; Protease; Reference proteome;
KW Serine protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..438
FT /note="Rhomboid-related protein 1"
FT /id="PRO_0000206173"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 312
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 377
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..77
FT /note="MGRVEDGGTTEELEDWDPGTSALPAPGIKQGPREQTGTGPLSQKCWEPEPDA
FT PSQPGPALWSRGRARTQALAGGSSL -> MDRSSLLQLIQE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9662444"
FT /id="VSP_005372"
SQ SEQUENCE 438 AA; 48314 MW; A7644AD39644A2F6 CRC64;
MGRVEDGGTT EELEDWDPGT SALPAPGIKQ GPREQTGTGP LSQKCWEPEP DAPSQPGPAL
WSRGRARTQA LAGGSSLQQL DPENTGFIGA DTFTGLVHSH ELPLDPAKLD MLVALAQSNE
QGQVCYQELV DLISSKRSSS FKRAIANGQR ALPRDGPLDE PGLGVYKRFV RYVAYEILPC
EVDRRWYFYR HRSCPPPVFM ASVTLAQIIV FLCYGARLNK WVLQTYHPEY MKSPLVYHPG
HRARAWRFLT YMFMHVGLEQ LGFNALLQLM IGVPLEMVHG LLRISLLYLA GVLAGSLTVS
ITDMRAPVVG GSGGVYALCS AHLANVVMNW AGMRCPYKLL RMVLALVCMS SEVGRAVWLR
FSPPLPASGP QPSFMAHLAG AVVGVSMGLT ILRSYEERLR DQCGWWVVLL AYGTFLLFAV
FWNVFAYDLL GAHIPPPP
